ID A0A089I1C3_9BACL Unreviewed; 887 AA.
AC A0A089I1C3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=DNA polymerase I {ECO:0000256|ARBA:ARBA00020311, ECO:0000256|RuleBase:RU004460};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417, ECO:0000256|RuleBase:RU004460};
GN Name=polA {ECO:0000256|RuleBase:RU004460};
GN ORFNames=H70357_11315 {ECO:0000313|EMBL:AIQ17182.1};
OS Paenibacillus sp. FSL H7-0357.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1536774 {ECO:0000313|EMBL:AIQ17182.1, ECO:0000313|Proteomes:UP000029508};
RN [1] {ECO:0000313|EMBL:AIQ17182.1, ECO:0000313|Proteomes:UP000029508}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL H7-0357 {ECO:0000313|EMBL:AIQ17182.1,
RC ECO:0000313|Proteomes:UP000029508};
RA den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT "Comparative genomics of the Paenibacillus odorifer group.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: In addition to polymerase activity, this DNA polymerase
CC exhibits 5'-3' exonuclease activity. {ECO:0000256|RuleBase:RU004460}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC Evidence={ECO:0000256|ARBA:ARBA00024632,
CC ECO:0000256|RuleBase:RU004460};
CC -!- SUBUNIT: Single-chain monomer with multiple functions.
CC {ECO:0000256|ARBA:ARBA00011541, ECO:0000256|RuleBase:RU004460}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-A family.
CC {ECO:0000256|ARBA:ARBA00007705, ECO:0000256|RuleBase:RU004460}.
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DR EMBL; CP009241; AIQ17182.1; -; Genomic_DNA.
DR RefSeq; WP_038588972.1; NZ_CP009241.1.
DR AlphaFoldDB; A0A089I1C3; -.
DR STRING; 1536774.H70357_11315; -.
DR KEGG; paeh:H70357_11315; -.
DR eggNOG; COG0258; Bacteria.
DR eggNOG; COG0749; Bacteria.
DR HOGENOM; CLU_004675_0_0_9; -.
DR Proteomes; UP000029508; Chromosome.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR CDD; cd08637; DNA_pol_A_pol_I_C; 1.
DR CDD; cd06140; DNA_polA_I_Bacillus_like_exo; 1.
DR CDD; cd09898; H3TH_53EXO; 1.
DR CDD; cd09859; PIN_53EXO; 1.
DR Gene3D; 3.30.70.370; -; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
DR Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR002562; 3'-5'_exonuclease_dom.
DR InterPro; IPR020046; 5-3_exonucl_a-hlix_arch_N.
DR InterPro; IPR002421; 5-3_exonuclease.
DR InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR InterPro; IPR019760; DNA-dir_DNA_pol_A_CS.
DR InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR020045; DNA_polI_H3TH.
DR InterPro; IPR018320; DNA_polymerase_1.
DR InterPro; IPR002298; DNA_polymerase_A.
DR InterPro; IPR008918; HhH2.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR NCBIfam; TIGR00593; pola; 1.
DR PANTHER; PTHR10133; DNA POLYMERASE I; 1.
DR PANTHER; PTHR10133:SF62; DNA POLYMERASE THETA; 1.
DR Pfam; PF01367; 5_3_exonuc; 1.
DR Pfam; PF02739; 5_3_exonuc_N; 1.
DR Pfam; PF00476; DNA_pol_A; 1.
DR PRINTS; PR00868; DNAPOLI.
DR SMART; SM00474; 35EXOc; 1.
DR SMART; SM00475; 53EXOc; 1.
DR SMART; SM00279; HhH2; 1.
DR SMART; SM00482; POLAc; 1.
DR SUPFAM; SSF47807; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF88723; PIN domain-like; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS00447; DNA_POLYMERASE_A; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU004460};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU004460};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|RuleBase:RU004460};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004460};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|RuleBase:RU004460}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004460};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 2..260
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 305..477
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 644..851
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 887 AA; 98566 MW; 578863E0FBADB248 CRC64;
MDKLILIDGN NIIYRAFFAM PPLTNTAGQQ TNAVYGFTTM LLRLIEEHKP SHLIVAFDAG
KITFRHEGYE DYKGGRQKTP PELSEQFPML KDLLRDMGVP QFEISGYEAD DIIGSISREA
DEAGRQVMIV SGDKDMLQLA SEYTTVALVR KGVTEVELYG PQQIREKYDL TPEQIIDLKG
LMGDASDNIP GVPGVGEKTA LKLLHQFGSV EGVLAGTGEL KGKMKEKLEE HADSAVMSKK
LATIYREVPL EHAWEDMEFT GIKGDTAGPA LAKLEFKSLL ERLSLSAYSP SSDGAVEAVE
AAVLDITIVG ESELEDLISA LPGISALHVE SNGENPHRAE VIGLGLSSPE RHYFVPFALL
QSHAAAPLRA WLGDSKAPKS GYDLHRADLA LHWQGIPFAG AANDVQLAAY LLDPTEANQN
LNDLTAKYGL PRLSPDEEVF GKGAKYKIPE LEILGNHVAR KSATVLGIVE KQQQELTETA
MTGLFEDLEM PLSRILADME KQGIAVNKED LKELGKEFEA QISKLVAEIY EICGTEFNLN
SPKQLGEILF VKLGLPVVKK TKTGYSTDAE VLEKLAPYHD VVRLILQYRS IAKLQSTYVE
GLLKEVSEVT GKVHTFYRQT IAATGRLSSQ FPNLQNIPIR LEEGRKIRKV FVPSEPGWSI
LAADYSQIEL RVLAHISGDE RMKEAFLHDM DIHTKTAMDV FGVTADQVDS NMRRSAKAVN
FGIVYGISDY GLSQNLGISR KEASHFIEQY FEVYEGVRRY MDDIVLDARK QGYVTTLLER
RRYLPEINAK NFNLRSFAER TAMNTPIQGT AADIIKLAMV HMDKALYERG LKSRMLLQVH
DELVFEVPED ELELMKELLP KVMAGALKLS VPLKAEVSYG SNWYEAK
//